Mouse IgG2 ELISA KIT

Species :

Mouse

Assay Type :

Solid Phase Sandwich ELISA

Sensitivity :

2 ng/ml

Detection Range :

7.8-250 ng/ml

Assay Length :

3.5h

Sample Type :

Serum, plasma, Cell culture supernatant

Long Name :

Total Immunoglobulin G2

Synonyms :

IgG2

Background :

Immunoglobulin G (IgG) is antibody molecule. Each IgG is composed of four peptide chains — two heavy chains γ and two light chains. IgG antibodies are large molecules of about 150 kDa composed of four peptide chains. It contains two identical class γ heavy chains of about 50 kDa and two identical light chains of about 25 kDa, thus a tetrameric quaternary structure. The two heavy chains are linked to each other and to a light chain each by disulfide bonds. The resulting tetramer has two identical halves, which together form the Y-like shape. Each end of the fork contains an identical antigen binding site. The Fc regions of IgGs bear a highly conserved N-glycosylation site. The N-glycans attached to this site are predominantly core-fucosylated diantennary structures of the complex type. In addition, small amounts of these N-glycans also bear bisecting GlcNAc and α-2, 6-linked sialic acid residues [1]. IgG antibodies are involved in predominantly the secondary immune response. The presence of specific IgG, in general, corresponds to maturation of the antibody response [2]. IgG can bind to many kinds of pathogens, for example viruses, bacteria, and fungi, and protects the body against them by agglutination and immobilization, complement activation (classical pathway), opsonization for phagocytosis, and neutralization of their toxins. There are four IgG subclasses (IgG1, 2, 3, and 4) in humans, named in order of their abundance in serum (IgG2 being the second most abundant). The relative ability of different IgG subclasses to fix complement may explain why some anti-donor antibody responses do harm a graft after organ transplantation.[3] In a mouse model of autoantibody mediated anemia using IgG isotype switch variants of an anti-erythrocytes autoantibody, it was found that mouse IgG2a was superior to IgG1 in activating complement. Moreover, it was found that the IgG2a isotype was able to interact very efficiently with FcgammaR. As a result, 20 times higher doses of IgG1, in relationship to IgG2a autoantibodies, were required to induce autoantibody mediated pathology.[